HPA001400
Anti-IMPDH2 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-IMP dehydrogenase 2 antibody produced in rabbit, Anti-IMPD 2 antibody produced in rabbit, Anti-IMPDH-II antibody produced in rabbit, Anti-Inosine-5′-monophosphate dehydrogenase 2 antibody produced in rabbit
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About This Item
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human
enhanced validation
RNAi knockdown
Learn more about Antibody Enhanced Validation
technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000
immunogen sequence
GFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKD
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... IMPDH2(3615)
Related Categories
Immunogen
Inosine-5′-monophosphate dehydrogenase 2 recombinant protein epitope signature tag (PrEST)
Application
Anti-IMPDH2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
IMPDH2 (inosine 5′-monophosphate dehydrogenase 2) encodes a rate-limiting enzyme involved in the de novo guanine nucleotide biosynthesis that catalyzes the NAD-dependent oxidation of inosine-5′-monophosphate (IMP) into xanthine-5′-monophosphate (XMP). It maintains the cellular guanine deoxy- and ribonucleotide pools that are required for the synthesis of DNA and RNA. It may be involved in some tumor progression and malignancy and may serve as a target for anticancer and immunosuppressive chemotherapy as it catalyzes an important step in purine nucleotide biosynthesis, which is necessary for the proliferation of lymphocytes.
Features and Benefits
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Linkage
Corresponding Antigen APREST83044
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
M D Sintchak et al.
Immunopharmacology, 47(2-3), 163-184 (2000-07-06)
The enzyme IMPDH is a homotetramer of approximately 55 kDa subunits and consists of a (beta/alpha)(8) barrel core domain and a smaller subdomain. The active site has binding pockets for the two substrates IMP and NAD. The enzymatic reaction of
Anna Bianchi-Smiraglia et al.
Nature methods, 14(10), 1003-1009 (2017-09-05)
GTP is a major regulator of multiple cellular processes, but tools for quantitative evaluation of GTP levels in live cells have not been available. We report the development and characterization of genetically encoded GTP sensors, which we constructed by inserting
Stefan J Barfeld et al.
Oncotarget, 6(14), 12587-12602 (2015-04-15)
The androgen receptor is a key transcription factor contributing to the development of all stages of prostate cancer (PCa). In addition, other transcription factors have been associated with poor prognosis in PCa, amongst which c-Myc (MYC) is a well-established oncogene
Joseph A Wawrzyniak et al.
Cell reports, 5(2), 493-507 (2013-10-22)
Melanoma is one of the most aggressive types of human cancers, and the mechanisms underlying melanoma invasive phenotype are not completely understood. Here, we report that expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of
Sudha Mannava et al.
Cell cycle (Georgetown, Tex.), 7(15), 2392-2400 (2008-08-05)
To identify C-MYC targets rate-limiting for proliferation of malignant melanoma, we stably inhibited C-MYC in several human metastatic melanoma lines via lentivirus-based shRNAs approximately to the levels detected in normal melanocytes. C-MYC depletion did not significantly affect levels of E2F1
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